Automatic Carbohydrate Analyzer Operation and Maintenance Manual.

Stevens, R.H.

doi:10.2172/4363381

Cited by 3 publications

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“…O monitoramento é realizado sobre o sinal do satélite Brasilsat B2 (ver tabela 1) recebido no Rio de Janeiro, porém em nível de frequência intermediária (FI -70Mhz), i.e., após o batimento com o oscilador local do transceiver [2].…”

Section: O Experimentounclassified

Efeitos Das Bolhas Ionosféricas nas Comunicações Via Satélite na Banda C

Soares¹

2001

Anais Do XIX Simpósio Brasileiro De Telecomunicações

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Esse artigo apresenta alguns resultados obtidos a partir da monitoração de um enlace do satélite Brasilsat B2 (Banda C). Os dados foram aquisitados por um sistema automatizado que registrou, o espectro de frequência do transponder 2A (3.74GHz a 3.78GHz), de 10 de outubro de 2000 a 15 de abril de 2001. Neste período registraram-se 37 anomalias noturnas no sinal, sendo 21 de forte intensidade e, dentre essas, 16 com mais de uma hora de duração. Por comparação com dados geofísicos confirmou-se que as anomalias no sinal foram causadas por depleções no plasma ionosférico, eventos mais conhecidos como Bolhas Ionosféricas. Para interpretação dos resultados contou-se com o apoio do Instituto Nacional de Pesquisas Espaciais (INPE).Em negrito : dias com ocorrência de Bolhas. Em itálico : dias em que o imageador não funcionou.

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Section: O Experimentounclassified

Efeitos Das Bolhas Ionosféricas nas Comunicações Via Satélite na Banda C

Soares¹

2001

Anais Do XIX Simpósio Brasileiro De Telecomunicações

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Analysis of Protein S‐Nitrosylation

Mannick

Schonhoff

2004

CP Protein Science

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S‐nitrosylation is the binding of an NO group to a cysteine or other thiol. Like phosphorylation, S‐nitrosylation is a precisely targeted and rapidly reversible post‐translational modification that serves as an on/off switch for protein function during cell signaling. However, unlike phosphorylation, S‐nitrosylation of proteins occurs nonenzymatically, mediated, at least in part, by redox‐regulated chemical reactions in cells. Alterations in pH, pO2, cellular reductants, transition metals, and UV light lead to the loss and/or gain of S‐NO bonds. Due to the redox‐sensitive nature of the modification, analysis of protein S‐nitrosylation is technically difficult, the S‐NO bond formation being easily disrupted during sample preparation. In addition, the level of S‐nitrosylated proteins in cells approaches the limit of detection of currently available technology. Despite these technical challenges, several useful methods have been developed recently to measure protein S‐nitrosylation in biologic samples, and these are described in this unit.

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Analysis of Protein S‐Nitrosylation

Mannick

Schonhoff

2006

CP Protein Science

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S-nitrosylation is the binding of an NO group to a cysteine or other thiol. Like phosphorylation, S-nitrosylation is a precisely targeted and rapidly reversible post-translational modification that serves as an on/off switch for protein function during cell signaling. However, unlike phosphorylation, S-nitrosylation of proteins occurs nonenzymatically and is mediated, at least in part, by redox-regulated chemical reactions in cells. Alterations in pH, pO(2), cellular reductants, transition metals, and UV light lead to the loss and/or gain of S-NO bonds. Due to the redox-sensitive nature of the modification, analysis of protein S-nitrosylation is technically difficult, since the S-NO bond is easily disrupted during sample preparation. In addition, the level of S-nitrosylated proteins in cells approaches the limit of detection of currently available technology. Despite these technical challenges, several useful methods have been developed recently to measure protein S-nitrosylation in biological samples, and these are described in this unit.

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Automatic Carbohydrate Analyzer Operation and Maintenance Manual.

Cited by 3 publications

References 0 publications

Efeitos Das Bolhas Ionosféricas nas Comunicações Via Satélite na Banda C

Efeitos Das Bolhas Ionosféricas nas Comunicações Via Satélite na Banda C

Analysis of Protein S‐Nitrosylation

Analysis of Protein S‐Nitrosylation

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